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Perforins | SpringerLink
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“Perforins” – cytotoxic cell perforin-1, proteins contributing to the complement membrane attack complex (MAC) and other perforin-like proteins – form unconventional pores in biological membranes in the sense that as well as a ring of subunits...
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Keywords {π}
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Topics {βοΈ}
month download article/chapter garcia-saez aj perforin-mediated target-cell death phospholipid-binding c2 domain myd88-dependent signaling pathway form widely-varying sizes beta-sheet transition identified resulting arc-pore structures membrane attack complex/perforin glial-guided neuronal migration binary pore-forming proteins bax central helices perforin-mediated myocardial damage cytolytic pore-forming protein cell-membrane pores induced c8alpha-macpf reveals mechanism purified pore-forming protein ion channel-forming properties bacterial toxin pneumolysin bacterial cholesterol-dependent cytolysin cytotoxic t-cell granules perforin-related protein pleurotolysin facilitate rapid access plasma membrane repair pore-forming toxin privacy choices/manage cookies membrane attack complex conductance fluctuations induced device instant download eukaryotic protein toxin editor information editors persechini pm induce cell death regulate drosophila growth ojcius dm pore-forming toxins pore-forming protein sonnen af macpf/cdc family shepard la pore-forming proteins macpf/cdc proteins cytolytic pore lined killer cell attack calcium-dependent permeabilization peptide-induced pores rapid membrane disruption membrane-spanning domain endosomal membrane trigger mitochondrial outer membrane
Questions {β}
- Teissie J, Golzio M, Rols MP (2005) Mechanisms of cell membrane electropermeabilization: a minireview of our present (lack of ?
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ScholarlyArticle:
headline:Perforins
pageEnd:312
pageStart:289
image:https://media.springernature.com/w153/springer-static/cover/book/978-3-319-20149-8.jpg
genre:
Biomedical and Life Sciences
Biomedical and Life Sciences (R0)
isPartOf:
name:Electrophysiology of Unconventional Channels and Pores
isbn:
978-3-319-20149-8
978-3-319-20148-1
type:Book
publisher:
name:Springer International Publishing
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
type:Organization
author:
name:Robert J. C. Gilbert
affiliation:
name:Wellcome Trust Centre for Human Genetics, University of Oxford
address:
name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
type:PostalAddress
type:Organization
email:[email protected]
type:Person
keywords:Perforin, Complement membrane attack complex, Toroidal pore, Proteolipidic pore, Single channel conductance
description:βPerforinsβ β cytotoxic cell perforin-1, proteins contributing to the complement membrane attack complex (MAC) and other perforin-like proteins β form unconventional pores in biological membranes in the sense that as well as a ring of subunits circumscribing an opening in the lipid bilayer, arcs of subunits induce similar effects. The resulting arc-pore structures are completed by a lipidic edge, conferring distinctive functional characteristics on them. Electrophysiological measurements have played a distinguished role in the discovery and characterisation of this alternative mechanism of pore formation which enables the same protein to form widely-varying sizes of pore and enact a greater diversity of effects than more conventional channels. This review discusses the mechanism of pore formation by the perforins and the way in which it has been illuminated by electrical conductance studies alongside imaging methods such as electron microscopy and atomic force microscopy.
datePublished:2015
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name:Wellcome Trust Centre for Human Genetics, University of Oxford
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name:Robert J. C. Gilbert
affiliation:
name:Wellcome Trust Centre for Human Genetics, University of Oxford
address:
name:Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK
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